PKC-dependent phosphorylation of the p97 repressor regulates the transcription of aldolase A L-type promoter

FEBS Lett. 1999 Jul 2;454(1-2):61-6. doi: 10.1016/s0014-5793(99)00775-9.

Abstract

Expression of mouse aldolase A L-type mRNA is negatively modulated by a cis element (AldA-NRE), located within the aldolase A distal promoter (pL). AldA-NRE interacts with a 97-kDa repressor protein (p97), which binds DNA in a cell cycle-dependent manner. We demonstrate that the binding between AldA-NRE and p97 decreases during differentiation of human Caco-2 cells and is inversely correlated with L-type mRNA expression. Phosphorylation of the p97 repressor weakened its DNA binding activity in differentiated Caco-2 cells, while dephosphorylation enhanced the binding in proliferating cells. Stimulation of protein kinase C (PKC) in vivo decreased the binding of p97 to AldA-NRE and stimulated transcription, while inhibition of PKC stimulated p97 binding and downregulated transcription. These findings suggest that PKC is a mediator of the binding and silencing function of the p97/AldA-NRE repressor complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Caco-2 Cells
  • Dose-Response Relationship, Drug
  • Fructose-Bisphosphate Aldolase / genetics*
  • Humans
  • Mice
  • Models, Biological
  • Nuclear Proteins / chemistry
  • Phosphorylation
  • Promoter Regions, Genetic*
  • Protein Kinase C / metabolism*
  • Recombinant Fusion Proteins
  • Repressor Proteins / chemistry*
  • Time Factors
  • Transcription, Genetic*

Substances

  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Protein Kinase C
  • Fructose-Bisphosphate Aldolase